Nicotinamide reduced form

Diphosphopyridine nucleotide, reduced form Adenine-D-ribose-phosphate-phosphate D-ribose-nicotinamide, reduced form Cozymase, reduced form... 

Ammonia reacts with the ketone carbonyl group to give an mine (C=NH) which is then reduced to the amine function of the a ammo acid Both mine formation and reduc tion are enzyme catalyzed The reduced form of nicotinamide adenine diphosphonu cleotide (NADPH) is a coenzyme and acts as a reducing agent The step m which the mine is reduced is the one m which the chirality center is introduced and gives only L glutamic acid... 

NADH is the reduced form of nicotinamide adenine dinucleotide. 

Nicotinamide is an essential part of two important coenzymes nicotinamide adenine dinucleotide (NAD ) and nicotinamide adenine dinucleotide phosphate (NADP ) (Figure 18.19). The reduced forms of these coenzymes are NADH and NADPH. The nieotinamide eoenzymes (also known as pyridine nucleotides) are electron carriers. They play vital roles in a variety of enzyme-catalyzed oxidation-reduction reactions. (NAD is an electron acceptor in oxidative (catabolic) pathways and NADPH is an electron donor in reductive (biosynthetic) pathways.) These reactions involve direct transfer of hydride anion either to NAD(P) or from NAD(P)H. The enzymes that facilitate such... 

Several other electron-transfer reagents have been tested with arenediazonium ions, for example, A-benzyl-l,4-dihydronicotinamide, which is a model for biochemical reductions by NAD(P)H, the reduced form of NADP+ (nicotinamide adenine cfinucleotide phosphate) (Yasui et al., 1984). 

NADPH—p-Nicotinamide adenine-dinucleotide phosphate, reduced form. 

Figure 18.2 Summary of respiratory energy flows. Foods ate converted into the reduced form of nicotinamide adenine dinucleotide (NADH), a strong reductant, which is the most reducing of the respiratory electron carriers (donors). Respiration can he based on a variety of terminal oxidants, such as O2, nitrate, or fumarate. Of those, O2 is the strongest, so that aerobic respiration extracts the largest amount of free energy from a given amount of food. In aerobic respiration, NADH is not oxidized directly by O2 rather, the reaction proceeds through intermediate electron carriers, such as the quinone/quinol couple and cytochrome c. The most efficient respiratory pathway is based on oxidation of ferrocytochrome c (Fe ) with O2 catalyzed by cytochrome c oxidase (CcO). Of the 550 mV difference between the standard potentials of c)Tochrome c and O2, CcO converts 450 mV into proton-motive force (see the text for further details).

P. Mitchell (Nobel Prize for Chemistry, 1978) explained these facts by his chemiosmotic theory. This theory is based on the ordering of successive oxidation processes into reaction sequences called loops. Each loop consists of two basic processes, one of which is oriented in the direction away from the matrix surface of the internal membrane into the intracristal space and connected with the transfer of electrons together with protons. The second process is oriented in the opposite direction and is connected with the transfer of electrons alone. Figure 6.27 depicts the first Mitchell loop, whose first step involves reduction of NAD+ (the oxidized form of nicotinamide adenosine dinucleotide) by the carbonaceous substrate, SH2. In this process, two electrons and two protons are transferred from the matrix space. The protons are accumulated in the intracristal space, while electrons are transferred in the opposite direction by the reduction of the oxidized form of the Fe-S protein. This reduces a further component of the electron transport chain on the matrix side of the membrane and the process is repeated. The final process is the reduction of molecular oxygen with the reduced form of cytochrome oxidase. It would appear that this reaction sequence includes not only loops but also a proton pump, i.e. an enzymatic system that can employ the energy of the redox step in the electron transfer chain for translocation of protons from the matrix space into the intracristal space. 

Photosynthesis in green plants occurs in two basic processes. In the dark (the Calvin cycle) carbon dioxide is reduced by a strong reducing agent, the reduced form of nicotinamide adeninedinucleotide phosphate, NADPH2, with the help of energy obtained from the conversion of ATP to ADP ... 

A coenzyme is an organic compound that activates the primary enzyme to a catalytically active form. A coenzyme may act as a cofactor (see footnote 2), but the converse is not necessarily true. For example, the coenzyme nicotinamide adenine dinucleotide, in either its oxidized or reduced forms (NAD+ or NADH), often participates as a cofactor in enzyme reactions. 

The most important coenzymes in synthetic organic chemistry [14] and industrially applied biotransformations [15] are the nicotinamide cofactors NAD/ H (3a/8a, Scheme 43.1) and NAD(P)/H (3b/8b, Scheme 43.1). These pyridine nucleotides are essential components of the cell [16]. In all the reactions where they are involved, they serve solely as hydride donors or acceptors. The oxidized and reduced form of the molecules are shown in Scheme 43.1, the redox reaction taking place at the C-4 atom of the nicotinamide moiety. 

Endogenous NO is produced almost exclusively by L-arginine catabolism to L-citrul-line in a reaction catalyzed by a family of nitric oxide synthases (NOSs) [3]. In the first step, Arg is hydroxylated to an enzyme-bound intermediate "-hydroxy-1.-arginine (NHA), and 1 mol of NADPH (nicotinamide adenine dinucleotide phosphate, reduced form) and O2 are consumed. In the second step, N H A is oxidized to citrulline and NO, with consumption of 0.5 mol of NADPH and 1 mol of 02 (Scheme 1.1). Oxygen activation in both steps is carried out by the enzyme-bound heme, which derives electrons from NADPH. Mammalian NOS consists of an N-terminal oxy-... 

It is possible to use isolated, partially purified enzymes (dehydrogenases) for the reduction of ketones to optically active secondary alcohols. However, a different set of complications arises. The new C H bond is formed by delivery of the hydrogen atom from an enzyme cofactor, nicotinamide adenine dinucleotide (phosphate) NAD(P) in its reduced form. The cofactor is too expensive to be used in a stoichiometric quantity and must be recycled in situ. Recycling methods are relatively simple, using a sacrificial alcohol, or a second enzyme (formate dehydrogenase is popular) but the real and apparent complexity of the ensuing process (Scheme 8)[331 provides too much of a disincentive to investigation by non-experts. 

For the formation of one 02 molecule four electrons have to be transferred. This requires a "quantum storage device". In the photosynthetic system of green plants this is achieved with two photosystems that are linked through an electron transport chain, Fig. 10.2, and by means of the thylakoid-membrane that enables the separation of the photoproducts 02 and the reduced form of nicotinamide adenine dinucleotide phosphate, NADPH. 

NADH p-nicotinamide adenine dinucleotide, reduced form... 

Figure 6.1 Pathways involved in glucose oxidation by plant cells (a) glycolysis, (b) Krebs cycle, (c) mitochondrial cytochrome chain. Under anoxic conditions. Reactions 1, 2 and 3 of glycolysis are catalysed by lactate dehydrogenase, pyruvate decarboxylase and alcohol dehydrogenase, respectively. ATP and ADP, adenosine tri- and diphosphate NAD and NADHa, oxidized and reduced forms of nicotinamide adenine dinucleotide PGA, phosphoglyceraldehyde PEP, phosphoenolpyruvate Acetyl-CoA, acetyl coenzyme A FP, flavoprotein cyt, cytochrome e, electron. (Modified from Fitter and Hay, 2002). Reprinted with permission from Elsevier...

Although the structures for molecules having niacin activity are simple, the forms in which they act in human biochemistry are not so simple. Nicotinic acid and nicotinamide are precursors for three complex coenzymes in multiple oxida-tion/reduction (redox) reactions nicotinamide mononucleotide, NMN nicotinamide adenine dinucleotide, NAD+ and nicotinamide adenine dinucleotide phosphate, NADP. I shall use NAD+ as representative of the class. NADH is the corresponding reduced form. ... 

NMN is basically half of the NAD+ molecule nicotinamide ribose phosphate. NADP+ is NAD+ bearing a phosphate group at C3 of the ribose group attached to the adenine. The redox chemistry is the same in all three forms of the coenzymes. NAD+ is the form most frequently employed for biochemical oxidation reactions in catabohsm and NADP+ (in its reduced form NADPH) is the form usually employed for biochemical reduction reactions in anabohsm. NMN is employed infrequently. 

The pyridine nucleotides NAD and NADP always function in unbound form. The oxidized forms contain an aromatic nicotinamide ring in which the positive charge is delocalized. The right-hand example of the two resonance structures shown contains an electron-poor, positively charged C atom at the para position to nitrogen. If a hydride ion is added at this point (see above), the reduced forms NADH or NADPH arise. No radical intermediate steps occur. Because a proton is released at the same time, the reduced pyridine nucleotide coenzymes are correctly expressed as NAD(P)H+HT... 

At a later stage, Girotti et al. developed a highly sensitive and rapid bioluminescence flow-through sensor for the determination of the L-phenyl-alanine (Phe) in serum by monitoring the reduced form of nicotinamide... 

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